Thioredoxin and Related Molecules–From Biology to Health and Disease

The hallmarks of cancer

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Aging: a theory based on free radical and radiation chemistry

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Detection and isolation of type C retrovirus particles from fresh and cultured lymphocytes of a patient with cutaneous T-cell lymphoma

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Physiological functions of thioredoxin and thioredoxin reductase

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Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1

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Adult T-cell leukemia: clinical and hematologic features of 16 cases

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Induction of Apoptosis by ASK1, a Mammalian MAPKKK That Activates SAPK/JNK and p38 Signaling Pathways

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THIOREDOXIN

Holmgren, A. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.001321 · Cited by 1,955

Oxidative stress in neurodegeneration: Cause or consequence?

Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869

Thioredoxin and Glutaredoxin Systems

Holmgren, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71625-6 · Cited by 1,804

Antioxidants Maintain Cellular Redox Homeostasis by Elimination of Reactive Oxygen Species

He, L., He, T., Farrar, S., Ji, L., Liu, T., & Ma, X. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000485089 · Cited by 2,207

The thioredoxin antioxidant system

Lu, J., & Holmgren, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.036 · Cited by 2,055

Redox regulation of cell survival

Trachootham, D., Lu, W., Ogasawara, M. A., Valle, N. R.-D., & Huang, P. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1957 · Cited by 1,781

Histone deacetylase inhibitors: molecular mechanisms of action

Xu, W. S., Parmigiani, R. B., & Marks, P. A. (2007) · Oncogene · doi:10.1038/sj.onc.1210620 · Cited by 1,542

Selenium in human health and disease

Fairweather-Tait, S. J., Bao, Y., Broadley, M. R., Collings, R., Ford, D., Hesketh, J. E., & Hurst, R. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3275 · Cited by 1,330

Radical-free biology of oxidative stress

Jones, D. P. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00283.2008 · Cited by 1,213

The molecular basis of retinal ganglion cell death in glaucoma

Almasieh, M., Wilson, A. M., Morquette, B., Vargas, J. L. C., & Polo, A. D. (2011) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2011.11.002 · Cited by 990

Thioredoxins, Glutaredoxins, and Peroxiredoxins—Molecular Mechanisms and Health Significance: from Cofactors to Antioxidants to Redox Signaling

Hanschmann, E.-M., Godoy, J. R., Berndt, C., Hudemann, C., & Lillig, C. H. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4599 · Cited by 696

Focus on mammalian thioredoxin reductases — Important selenoproteins with versatile functions

Arnér, E. S. J. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.01.014 · Cited by 696

Protein Disulfide Isomerase: A Critical Evaluation of Its Function in Disulfide Bond Formation

Hatahet, F., & Ruddock, L. W. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2466 · Cited by 673

Selenoproteins

Lu, J., & Holmgren, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800045200 · Cited by 618

Oxygen Consumption and Usage During Physical Exercise: The Balance Between Oxidative Stress and ROS-Dependent Adaptive Signaling

Radak, Z. O., Zhao, Z., Koltai, E., Ohno, H., & Atalay, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4498 · Cited by 643

Is the oxidative stress theory of aging dead?

Pérez, V. I., Bokov, A., Remmen, H. V., Mele, J., Ran, Q., Ikeno, Y., & Richardson, A. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.06.003 · Cited by 604

The oxidative stress-inducible cystine/glutamate antiporter, system x c − : cystine supplier and beyond

Conrad, M., & Sato, H. (2011) · Amino Acids · doi:10.1007/s00726-011-0867-5 · Cited by 621

Thioredoxin reductase: A target for gold compounds acting as potential anticancer drugs

Bindoli, A., Rigobello, M. P., Scutari, G., Gabbiani, C., Casini, A., & Luigi Messori, A. (2009) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2009.02.026 · Cited by 608

Thioredoxin and thioredoxin reductase: Current research with special reference to human disease

Holmgren, A., & Lu, J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.03.083 · Cited by 577

Glutaredoxin systems

Lillig, C. H., Berndt, C., & Holmgren, A. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.06.003 · Cited by 582

Regulated Protein Denitrosylation by Cytosolic and Mitochondrial Thioredoxins

Benhar, M., Forrester, M. T., Hess, D. T., & Stamler, J. S. (2008) · Science · doi:10.1126/science.1158265 · Cited by 561

Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species

Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542

Mitohormesis: Promoting Health and Lifespan by Increased Levels of Reactive Oxygen Species (ROS)

Ristow, M., & Schmeisser, K. (2014) · Dose-Response · doi:10.2203/dose-response.13-035.ristow · Cited by 534

Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide

Lu, J., Chew, E.-H., & Holmgren, A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701549104 · Cited by 526

Molecular Mechanisms and Clinical Implications of Reversible Protein S -Glutathionylation

Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A., & Shelton, M. D. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2089 · Cited by 523

Protein denitrosylation: enzymatic mechanisms and cellular functions

Benhar, M., Forrester, M. T., & Stamler, J. S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2764 · Cited by 532

Redox regulation of immunometabolism

Muri, J., & Köpf, M. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-00478-8 · Cited by 519

Thioredoxins and Glutaredoxins: Unifying Elements in Redox Biology

Meyer, Y., Buchanan, B. B., Vignols, F., & Reichheld, J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134201 · Cited by 498

Inhibition of the Human Thioredoxin System

Carvalho, C. M. L., Chew, E., Hashemy, S. I., Lu, J., & Holmgren, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710133200 · Cited by 456

Thioredoxin and Thioredoxin Target Proteins: From Molecular Mechanisms to Functional Significance

Lee, S., Kim, S. M., & Lee, R. T. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4322 · Cited by 459

Paradoxical Roles of Antioxidant Enzymes: Basic Mechanisms and Health Implications

Lei, X. G., Zhu, J., Cheng, W.-H., Bao, Y., Ho, Y.-S., Reddi, A. R., Holmgren, A., & Arnér, E. S. J. (2015) · Physiological Reviews · doi:10.1152/physrev.00010.2014 · Cited by 455

The Ferredoxin/Thioredoxin System of Oxygenic Photosynthesis

Schürmann, P., & Buchanan, B. B. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1931 · Cited by 430

Hyperglycemia and Glycation in Diabetic Complications

Nègre‐Salvayre, A., Salvayre, R., Augè, N., Pamplona, R., & Portero‐Otín, M. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2484 · Cited by 426

Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism

Krauth‐Siegel, R. L., & Comini, M. A. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.03.006 · Cited by 414

Reactive oxygen species: Destroyers or messengers?

Bartosz, G. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.11.009 · Cited by 386

Thioredoxin/Txnip: Redoxisome, as a Redox Switch for the Pathogenesis of Diseases

Yoshihara, E., Masaki, S., Matsuo, Y., Chen, Z., Tian, H., & Yodoi, J. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00514 · Cited by 367

Mitochondrial Thiols in Antioxidant Protection and Redox Signaling: Distinct Roles for Glutathionylation and Other Thiol Modifications

Murphy, M. P. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4289 · Cited by 351

Melatonin signaling and cell protection function

Luchetti, F., Canonico, B., Betti, M., Arcangeletti, M., Pilolli, F., Piroddi, M., Canesi, L., Papa, S., & Galli, F. (2010) · The FASEB Journal · doi:10.1096/fj.10-154450 · Cited by 349

Oxidative stress in autoimmune rheumatic diseases

Smallwood, M. J., Nissim, A., Knight, A. R., Whiteman, M., Haigh, R. C., & Winyard, P. G. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.086 · Cited by 358

Nitric oxide signaling: Classical, less classical, and nonclassical mechanisms

Martínez-Ruiz, A., Cadenas, S., & Lamas, S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.010 · Cited by 340

Oxidative Stress in Autism Spectrum Disorder

Bjørklund, G., Meguid, N. A., El-Bana, M. A., Tinkov, A. A., Saad, K., Dadar, M., Hemimi, M., Skalny, A. V., Hosnedlová, B., Kizek, R., et al. (2020) · Molecular Neurobiology · doi:10.1007/s12035-019-01742-2 · Cited by 323

Carbon dots: Applications in bioimaging and theranostics

Boakye‐Yiadom, K. O., Kesse, S., Opoku‐Damoah, Y., Filli, M. S., Aquib, M., Maviah, M. B. J., Farooq, M. A., Mavlyanova, R., Raza, F., Bavi, R., et al. (2019) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2019.04.055 · Cited by 317

A high-throughput drug screen for Entamoeba histolytica identifies a new lead and target

Debnath, A., Parsonage, D., Andrade, R. M., He, C., Cobo, E. R., Hirata, K. K., Chen, S., García‐Rivera, G., Orozco, E., Martínez, M. B., et al. (2012) · Nature Medicine · doi:10.1038/nm.2758 · Cited by 307

The Thioredoxin System as a Therapeutic Target in Human Health and Disease

Mahmood, D. F. D., Abderrazak, A., Hadri, K. E., Simmet, T., & Rouis, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4757 · Cited by 311

The clinical development of histone deacetylase inhibitors as targeted anticancer drugs

Marks, P. (2010) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2010.510514 · Cited by 285

Thioredoxin System in Cell Death Progression

Lu, J., & Holmgren, A. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4650 · Cited by 279

Thioredoxins and glutaredoxins as facilitators of protein folding

Berndt, C., Lillig, C. H., & Holmgren, A. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.02.003 · Cited by 273

Enzymatic mechanisms regulating protein S-nitrosylation: implications in health and disease

Anand, P., & Stamler, J. S. (2012) · Journal of Molecular Medicine · doi:10.1007/s00109-012-0878-z · Cited by 277

Identification of oxadiazoles as new drug leads for the control of schistosomiasis

Sayed, A. A., Simeonov, A. M., Thomas, C. J., Inglese, J., Austin, C. P., & Williams, D. L. (2008) · Nature Medicine · doi:10.1038/nm1737 · Cited by 274

Oxidative stress, redox regulation and diseases of cellular differentiation

Ye, Z., Zhang, J., Townsend, D. M., & Tew, K. D. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.11.010 · Cited by 271

A redox-dependent mechanism for regulation of AMPK activation by thioredoxin1 during energy starvation

Shao, D., Oka, S.-I., Liu, T., Zhai, P., Ago, T., Sciarretta, S., Li, H., & Sadoshima, J. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2013.12.013 · Cited by 252

TrxR1 as a Potent Regulator of the Nrf2-Keap1 Response System

Cebula, M., Schmidt, E. E., & Arnér, E. S. J. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6378 · Cited by 251

Gold(I) Carbene Complexes Causing Thioredoxin 1 and Thioredoxin 2 Oxidation as Potential Anticancer Agents

Schuh, E., Pflüger, C., Citta, A., Folda, A., Rigobello, M. P., Bindoli, A., Casini, A., & Mohr, F. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300428v · Cited by 253

Thiol Chemistry in Peroxidase Catalysis and Redox Signaling

Bindoli, A., Fukuto, J. M., & Forman, H. J. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2063 · Cited by 247

Irreversible inhibition of cytosolic thioredoxin reductase 1 as a mechanistic basis for anticancer therapy

Stafford, W. C., Peng, X., Olofsson, M. H., Zhang, X., Luci, D. K., Lu, L., Cheng, Q., Tresaugues, L., Dexheimer, T. S., Coussens, N. P., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf7444 · Cited by 248

Glutathione and Glutaredoxin Act as a Backup of Human Thioredoxin Reductase 1 to Reduce Thioredoxin 1 Preventing Cell Death by Aurothioglucose

Du, Y., Zhang, H., Lu, J., & Holmgren, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.392225 · Cited by 230

Crystal Structure and Catalysis of the Selenoprotein Thioredoxin Reductase 1

Cheng, Q., Sandalova, T., Lindqvist, Y., & Arnér, E. S. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807068200 · Cited by 227

Diabetic cataracts: mechanisms and management

Obrosova, I. G., Chung, S. S. M., & Kador, P. F. (2010) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.1075 · Cited by 237

From structure to redox: The diverse functional roles of disulfides and implications in disease

Bechtel, T. J., & Weerapana, E. (2017) · PROTEOMICS · doi:10.1002/pmic.201600391 · Cited by 227

Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals

Kim, H., & Gladyshev, V. N. (2007) · Biochemical Journal · doi:10.1042/bj20070929 · Cited by 204

Redox outside the Box: Linking Extracellular Redox Remodeling with Intracellular Redox Metabolism

Banerjee, R. V. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.287995 · Cited by 211

Biomarkers of mercury toxicity: Past, present, and future trends

Branco, V., Caito, S., Farina, M., da Rocha, J. B. T., Aschner, M., & Carvalho, C. M. L. (2017) · Journal of Toxicology and Environmental Health Part B · doi:10.1080/10937404.2017.1289834 · Cited by 204

Thioredoxin Interacting Protein: Redox Dependent and Independent Regulatory Mechanisms

Spindel, O. N., WORLD, C., & Berk, B. C. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4137 · Cited by 192

Regulation of the Catalytic Activity and Structure of Human Thioredoxin 1 via Oxidation and S-Nitrosylation of Cysteine Residues

Hashemy, S. I., & Holmgren, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801047200 · Cited by 192

The thioredoxin/peroxiredoxin/sulfiredoxin system: current overview on its redox function in plants and regulation by reactive oxygen and nitrogen species

Sevilla, F., Camejo, D. M., Ortiz‐Espín, A., Calderón, A., Lázaro, J. J., & Jiménez, A. (2015) · Journal of Experimental Botany · doi:10.1093/jxb/erv146 · Cited by 195

Principles in Redox Signaling: From Chemistry to Functional Significance

Bindoli, A., & Rigobello, M. P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4655 · Cited by 194

Histone deacetylase inhibitors: A chemical genetics approach to understanding cellular functions

Marks, P. A. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.05.008 · Cited by 189

Mercury and selenium interaction in vivo: Effects on thioredoxin reductase and glutathione peroxidase

Branco, V., Canário, J., Lu, J., Holmgren, A., & Carvalho, C. M. L. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.12.002 · Cited by 186

Inhibition of bacterial thioredoxin reductase: an antibiotic mechanism targeting bacteria lacking glutathione

Lu, J., Vlamis‐Gardikas, A., Kandasamy, K., Zhao, R., Gustafsson, T. N., Engstrand, L. G., Hoffner, S., Engman, L., & Holmgren, A. (2012) · The FASEB Journal · doi:10.1096/fj.12-223305 · Cited by 183

Redox regulation of the immune response

Gostner, J. M., Becker, K., Fuchs, D., & Sucher, R. (2013) · Redox Report · doi:10.1179/1351000213y.0000000044 · Cited by 191

Viral-mediated RdCVF and RdCVFL expression protects cone and rod photoreceptors in retinal degeneration

Byrne, L. C., Dalkara, D., Luna, G., Fisher, S. K., Clérin, E., Sahel, J., Léveillard, T., & Flannery, J. G. (2014) · Journal of Clinical Investigation · doi:10.1172/jci65654 · Cited by 195

Reactive Oxygen Species and Aging in Caenorhabditis elegans : Causal or Casual Relationship?

Raamsdonk, J. M. V., & Hekimi, S. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3215 · Cited by 186

Recent developments in the synthesis of biologically relevant selenium-containing scaffolds

Banerjee, B., & Koketsu, M. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.03.008 · Cited by 180

Thiol redox homeostasis in neurodegenerative disease

McBean, G. J., Aslan, M., Griffiths, H. R., & Torrão, R. C. (2015) · Redox Biology · doi:10.1016/j.redox.2015.04.004 · Cited by 182

The structural basis for the negative regulation of thioredoxin by thioredoxin-interacting protein

Hwang, J., Suh, H., Jeon, Y. H., Hwang, E., Nguyen, L. T., Yeom, J., Lee, S., Lee, C., Kim, K. J., Kang, B. S., et al. (2014) · Nature Communications · doi:10.1038/ncomms3958 · Cited by 176

Thioredoxin Reductase Inhibition for Cancer Therapy

Gencheva, R., & Arnér, E. S. J. (2021) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-052220-102509 · Cited by 181

Crystal structure of the human thioredoxin reductase–thioredoxin complex

Fritz‐Wolf, K., Kehr, S., Stumpf, M., Rahlfs, S., & Becker, K. (2011) · Nature Communications · doi:10.1038/ncomms1382 · Cited by 173

Cell Death by SecTRAPs: Thioredoxin Reductase as a Prooxidant Killer of Cells

Anestål, K., Prast‐Nielsen, S., Čėnas, N., & Arnér, E. S. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001846 · Cited by 171

Protein-Thiol Oxidation and Cell Death: Regulatory Role of Glutaredoxins

Allen, E. M. G., & Mieyal, J. J. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4644 · Cited by 172

Molecular Mechanisms of Thioredoxin and Glutaredoxin as Hydrogen Donors for Mammalian S Phase Ribonucleotide Reductase

Avval, F. Z., & Holmgren, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809338200 · Cited by 169

Redox Proteomics in Selected Neurodegenerative Disorders: From Its Infancy to Future Applications

Butterfield, D. A., Marzia Perluigi, A., Reed, T. T., Muharib, T., Hughes, C. P., Robinson, R. A. S., & Rukhsana Sultana, A. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4109 · Cited by 171

Dual targeting of the thioredoxin and glutathione systems in cancer and HIV

Benhar, M., Shytaj, I. L., Stamler, J. S., & Savarino, A. (2016) · Journal of Clinical Investigation · doi:10.1172/jci85339 · Cited by 170

Protein Tyrosine Phosphorylation and Protein Tyrosine Nitration in Redox Signaling

Monteiro, H. P., Arai, R. J., & Travassos, L. R. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1853 · Cited by 158

Thioredoxin and Thioredoxin Reductase in Relation to Reversible S -Nitrosylation

Sengupta, R., & Holmgren, A. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4716 · Cited by 156

Cinnamaldehydes inhibit thioredoxin reductase and induce Nrf2: potential candidates for cancer therapy and chemoprevention

Chew, E., Nagle, A. A., Zhang, Y., Scarmagnani, S., Palaniappan, P. L. R. M., Bradshaw, T. D., Holmgren, A., & Westwell, A. D. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.028 · Cited by 152

The role of thioredoxin system in cancer: strategy for cancer therapy

Jia, J., Geng, W.-S., Wang, Z.-Q., Chen, L., & Zeng, X. (2019) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-019-03869-4 · Cited by 154

Emerging Role of Protein-Protein Transnitrosylation in Cell Signaling Pathways

Nakamura, T., & Lipton, S. A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4703 · Cited by 151

Glutaredoxins in Thiol/Disulfide Exchange

Lillig, C. H., & Berndt, C. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5007 · Cited by 145

Reactivity of Thioredoxin as a Protein Thiol-Disulfide Oxidoreductase

Cheng, Z., Zhang, J., Ballou, D. P., & Williams, C. H. (2011) · Chemical Reviews · doi:10.1021/cr100006x · Cited by 146

Altered redox state of monocytes from cryopyrin-associated periodic syndromes causes accelerated IL-1β secretion

Tassi, S., Carta, S., Delfino, L., Caorsi, R., Martini, A., Gattorno, M., & Rubartelli, A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000779107 · Cited by 141

The Disulfide Proteome and Other Reactive Cysteine Proteomes: Analysis and Functional Significance

Lindahl, M., Mata‐Cabana, A., & Kieselbach, T. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3551 · Cited by 142

Redox Regulation of DNA Repair: Implications for Human Health and Cancer Therapeutic Development

Luo, M., He, H., Kelley, M. R., & Georgiadis, M. M. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2698 · Cited by 140

Anti-oxidative, anti-cancer and anti-inflammatory actions by thioredoxin 1 and thioredoxin-binding protein-2

Watanabe, R., Nakamura, H., Masutani, H., & Yodoi, J. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.04.004 · Cited by 138

Effects of selenite and chelating agents on mammalian thioredoxin reductase inhibited by mercury: implications for treatment of mercury poisoning

Carvalho, C. M. L., Lu, J., Zhang, X., Arnér, E. S. J., & Holmgren, A. (2010) · The FASEB Journal · doi:10.1096/fj.10-157594 · Cited by 130

The thioredoxin-1 system is essential for fueling DNA synthesis during T-cell metabolic reprogramming and proliferation

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ROS-mediated inactivation of the PI3K/AKT pathway is involved in the antigastric cancer effects of thioredoxin reductase-1 inhibitor chaetocin

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